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P94248

- BGLFU_BIFBR

UniProt

P94248 - BGLFU_BIFBR

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Protein
Bifunctional beta-D-glucosidase/beta-D-fucosidase
Gene
N/A
Organism
Bifidobacterium breve
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Bifunctional beta-D-glucosidase/beta-D-fucosidase. Activity towards pNP-beta-D-fucoside is about 80-85% of the activity towards pNP-beta-D-glucoside. Also has slight activity (less than 10%) towards pNP-beta-D-galactoside, and very low activity (less than 1%) towards pNP-beta-D-xyloside. Hydrolyzes laminaribiose, sophorose, cellobiose and gentobiose. Not active against maltose, pNP-alpha-D-glucoside or pNP-beta-L-fucoside.2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.2 Publications
Hydrolysis of terminal non-reducing beta-D-fucose residues in beta-D-fucosides.2 Publications

Enzyme regulationi

Inhibited by Cu2+, Ag+ and Hg+, but not by other cations such as Mg2+, Ca2+, Mn2+ and Co2+. Inhibited by 1-amino-1-deoxy-D-glucose and p-chloromercuribenzoic acid, but not by EDTA or dithiothreitol. Inhibited by the disaccharides sucrose, lactose and cellobiose. The monosaccharides D-fructose, D-mannose, D-xylose and D-glucose increase the beta-D-fucosidase activity, but not the beta-D-glucosidase activity. D-glucose inhibits the beta-D-glucosidase activity, but promotes the beta-D-fucosidase activity. D-fucose inhibits the beta-D-glucosidase activity and does not significantly affect the beta-D-fucosidase activity.1 Publication

Kineticsi

  1. KM=1.3 mM for pNP-beta-D-glucoside2 Publications
  2. KM=0.7 mM for pNP-beta-D-fucoside1 Publication

pH dependencei

Optimum pH is 5.5 with pNP-beta-D-glucoside as a substrate. Retains more than 90% of its activity between pH 5.0 and 7.0. Retains 70% of its activity at pH 4.5 and 8.5.2 Publications

Temperature dependencei

Optimum temperature is 45 degrees Celsius with pNP-beta-D-glucoside as a substrate. Retains 60% of its activity after 10 minutes incubation at 50 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681Proton donor By similarityBy similarity
Active sitei362 – 3621Nucleophile By similarityBy similarity

GO - Molecular functioni

  1. beta-D-fucosidase activity Source: UniProtKB-EC
  2. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional beta-D-glucosidase/beta-D-fucosidase (EC:3.2.1.21, EC:3.2.1.38)
OrganismiBifidobacterium breve
Taxonomic identifieri1685 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 460459Bifunctional beta-D-glucosidase/beta-D-fucosidase1 Publication
PRO_0000395428Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP94248.
SMRiP94248. Positions 2-458.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P94248-1 [UniParc]FASTAAdd to Basket

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MTMIFPKGFM FGTATAAYQI EGAVAEGGRT PSIWDTFSHT GHTLNGDTGD    50
VADDFYHRWE DDLKLLRDLG VNAYRFSIGI PRVIPTPDGK PNQEGLDFYS 100
RIVDRLLEYG IAPIVTLYHW DLPQYMASGD GREGGWLERE TAYRIADYAG 150
IVAKCLGDRV HTYTTLNEPW CSAHLSYGGT EHAPGLGAGP LAFRAAHHLN 200
LAHGLMCEAV RAEAGAKPGL SVTLNLQICR GDADAVHRVD LIGNRVFLDP 250
MLRGRYPDEL FSITKGICDW GFVCDGDLDL IHQPIDVLGL NYYSTNLVKM 300
SDRPQFPQST EASTAPGASD VDWLPTAGPH TEMGWNIDPD ALYETLVRLN 350
DNYPGMPLVV TENGMACPDK VEVGTDGVKM VHDNDRIDYL RRHLEAVYRA 400
IEEGTDVRGY FAWSLMDNFE WAFGYSKRFG LTYVDYESQE RVKKDSFDWY 450
RRFIADHSAR 460
Length:460
Mass (Da):51,514
Last modified:May 1, 1997 - v1
Checksum:i5FD80CB8AB6888A9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D88311 Genomic DNA. Translation: BAA19881.1.
PIRiJC5137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D88311 Genomic DNA. Translation: BAA19881.1 .
PIRi JC5137.

3D structure databases

ProteinModelPortali P94248.
SMRi P94248. Positions 2-458.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR03356. BGL. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli."
    Nunoura N., Ohdan K., Tanaka K., Tamaki H., Yano T., Inui M., Yukawa H., Yamamoto K., Kumagai H.
    Biosci. Biotechnol. Biochem. 60:2011-2018(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "Purification and characterization of beta-D-glucosidase (beta-D-fucosidase) from Bifidobacterium breve clb acclimated to cellobiose."
    Nunoura N., Ohdan K., Yano T., Yamamoto K., Kumagai H.
    Biosci. Biotechnol. Biochem. 60:188-193(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-30, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiBGLFU_BIFBR
AccessioniPrimary (citable) accession number: P94248
Secondary accession number(s): O08487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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